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1jxt

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Revision as of 00:53, 10 September 2015

CRAMBIN MIXED SEQUENCE FORM AT 160 K. PROTEIN/WATER SUBSTATES

Structural highlights

1jxt is a 1 chain structure with sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1crn, 1cnr, 1ab1, 1cbn, 1jxu, 1jxw, 1jxx, 1jxy
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.

On the nature of a glassy state of matter in a hydrated protein: Relation to protein function.,Teeter MM, Yamano A, Stec B, Mohanty U Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:11572978^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Teeter MM, Yamano A, Stec B, Mohanty U. On the nature of a glassy state of matter in a hydrated protein: Relation to protein function. Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:11572978 doi:10.1073/pnas.201404398

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jxt"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1crn|1crn]], [[1cnr|1cnr]], [[1ab1|1ab1]], [[1cbn|1cbn]], [[1jxu|1jxu]], [[1jxw|1jxw]], [[1jxx|1jxx]], [[1jxy|1jxy]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jxt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jxt RCSB], [http://www.ebi.ac.uk/pdbsum/1jxt PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jxt OCA], [http://pdbe.org/1jxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jxt RCSB], [http://www.ebi.ac.uk/pdbsum/1jxt PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1jxt" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1jxt

From Proteopedia

Revision as of 00:53, 10 September 2015

CRAMBIN MIXED SEQUENCE FORM AT 160 K. PROTEIN/WATER SUBSTATES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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